ID Q1JVE4_DESA6 Unreviewed; 399 AA.
AC Q1JVE4;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN ORFNames=Dace_0061 {ECO:0000313|EMBL:EAT14214.1};
OS Desulfuromonas acetoxidans (strain DSM 684 / 11070).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Desulfuromonas.
OX NCBI_TaxID=281689 {ECO:0000313|EMBL:EAT14214.1, ECO:0000313|Proteomes:UP000005695};
RN [1] {ECO:0000313|EMBL:EAT14214.1, ECO:0000313|Proteomes:UP000005695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 684 / 11070 {ECO:0000313|Proteomes:UP000005695};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Desulfuromonas acetoxidans DSM
RT 684.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT14214.1, ECO:0000313|Proteomes:UP000005695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 684 / 11070 {ECO:0000313|Proteomes:UP000005695};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D.,
RA Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Desulfuromonas acetoxidans
RT DSM 684.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001197};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000860};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000256|ARBA:ARBA00005135}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000256|ARBA:ARBA00009184}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAT14214.1}.
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DR EMBL; AAEW02000042; EAT14214.1; -; Genomic_DNA.
DR RefSeq; WP_006003267.1; NZ_AAEW02000042.1.
DR AlphaFoldDB; Q1JVE4; -.
DR OrthoDB; 9792539at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000005695; Unassembled WGS sequence.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04870; ACT_PSP_1; 1.
DR CDD; cd07500; HAD_PSP; 1.
DR Gene3D; 3.30.70.260; -; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR InterPro; IPR049148; PSP_ACT.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR NCBIfam; TIGR00338; serB; 1.
DR PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR Pfam; PF13740; ACT_6; 1.
DR Pfam; PF21086; ACT_PSP_2; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01137; C1.6.1:_Phosphoserine_Phosphat; 1.
DR SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EAT14214.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005695};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 97..173
FT /note="Phosphoserine phosphatase ACT"
FT /evidence="ECO:0000259|Pfam:PF21086"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 399 AA; 43772 MW; E86568727731F782 CRC64;
MENRLILITI TGQDRPGVIA KVAQLIADTD GARIRDIEQT TTHTQMVLTL LLDLSAGGSS
EKPLIKDLLF QSKEMGLDLD FAVISEDEYR RKTAGNTYVV TILGSRVDAR SLAEVTGLLA
EASANVVRIS KLTQRELRCV ELLISTDGQL DIPALKRKLL QVGGSQRVDV AVQKERLYRR
AKRLVVMDMD STLIQVEVID ELARLAGVGE DVARITEQAM NGELDFGQSL AARVALLKGL
KEEALDEVYR SIPFTPGARN LVHILKRLGF RTAVISGGFK FFTDRLQQEL GLDYAFANQL
EIVNGEVTGR TMGRIVDGEC KAQLLEEIAE REGVTLDQVI AIGDGANDLP MLGKAGLGIA
FNAKARVREQ ADTHINQQSL DSILYLLGLS EREMDEISA
//
